BCAR1 is a ubiquitously expressed adaptor molecule originally identified as the major substrate of v-Src and v-Crk . p130Cas/BCAR1 belongs to the Cas family of adaptor proteins and can act as a docking protein for several signalling partners. Due to its ability to associate with multiple signaling partners, p130Cas/BCAR1 contributes to the regulation to a variety of signaling pathways leading to cell adhesion, migration, invasion, apoptosis, hypoxia and mechanical forces. p130Cas/BCAR1 plays a role in cell transformation and cancer progression and alterations of p130Cas/BCAR1 expression and the resulting activation of selective signalling are determinants for the occurrence of different types of human tumors. Due to the capacity of p130Cas/BCAR1, as an adaptor protein, to interact with multiple partners and to be regulated by phosphorylation and dephosphorylation, its expression and phosphorylation can lead to a wide range of functional consequences. Among the regulators of p130Cas/BCAR1 tyrosine phosphorylation, receptor tyrosine kinases (RTKs) and integrins play a prominent role. RTK-dependent p130Cas/BCAR1 tyrosine phosphorylation and the subsequent binding with specific downstream signaling molecule modulate cell processes such as actin cytoskeleton remodeling, cell adhesion, proliferation, migration, invasion and survival. Integrin-mediated p130Cas/BCAR1 phosphorylation upon adhesion to extracellular matrix (ECM) induces downstream signaling that is required for allowing cells to spread and migrate on the ECM. Both RTKs and integrin activation affect p130Cas/BCAR1 tyrosine phosphorylation and represent an efficient means by which cells utilize signals coming from growth factors and integrin activation to coordinate cell responses. Additionally, p130Cas/BCAR1 tyrosine phosphorylation on its substrate domain can be induced by cell stretching subsequent to changes in the rigidity of the extracellular matrix, allowing cells to respond to mechanical force changes in the cell environment.